Peptide properties

1Top 2Function-activity relationship 3Calculated physicochemical properties 4Peptide source & Food-borne protein(s) search 5Biological/Functional activity & target protein 6Taste properties & Structure 7Preparation method 8Stability & Cytotoxicity 9Additional information 10Database cross-references 11Reference(s)

List of peptide properties

DFBP ID - DFBPANHY0180(Antihypertensive peptide)

DFBP ID	DFBPANHY0180
Peptide sequence	FFVAPFPEVFGK
Type	Native peptide
Peptide/Function name	Antihypertensive peptide, CEI₁₂

Function-activity relationship

Main bioactivity	Antihypertensive activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Anticancer activity ^[D2], Antithrombotic activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Phe-Phe-Val-Ala-Pro-Phe-Pro-Glu-Val-Phe-Gly-Lys

Single-letter amino acid

FFVAPFPEVFGK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1384.63 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.8667^c

Hydrophilic residue ratio

83.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein
Precursor protein	α_s1-Casein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR7717 ---- Milk proteins ---- Alpha-S1-casein Source.2: DFBPPR8488 ---- Milk proteins ---- Alpha-S1-casein
Link-research Inductive analysis	Link 1: DFBPANHY0888----Milk Protein----α_s1-Casein

Biological/Functional activity & target protein

Antihypertensive activity	This peptide has potential antihypertensive activity.
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)NCC(=O)N[C@@]([H])(CCCCN)C(=O)O

Structure

Embedded Mol* Viewer

Docking

Embedded Mol* Viewer

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Milk proteins were hydrolyzed by trypsin from bovine pancreas.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	Non-Toxin
Prediction:	ToxinPred

Additional information

(1) ID₅₀ value (the concentration which inhibits 50% of the enzyme activity) of ACE inhibitor was calculated to be 77 μM.
(2) The use of a nisin as a ‘‘food-grade’’ inducer molecule, and generally-regarded-as-safe LAB species suggests that this system could be used for the production of functional food ingredients^[1].
(3) This peptide has the same structure as that reported for a bitter peptide ^[3].

Database cross-references

DFBP

[D1]	DFBPACEI0331
[D2]	DFBPANCA0110
[D3]	DFBPANTH0151
[D4]	DFBPMUFU0097

[D5]

[D6]

[D7]

[D8]

Reference(s)

Primary literature	Maruyama, S., Suzuki, H. A Peptide Inhibitor of Angiotensin I Converting Enzyme in the Tryptic Hydrolysate of Casein. Agricultural and Biological Chemistry. 2014, 46, 1393-4. DOI: 10.1080/00021369.1982.10865255
Other literature(s)	[1] Renye, J.A. and G.A. Somkuti, Nisin-induced expression of a recombinant antihypertensive peptide in dairy lactic acid bacteria. Biotechnology Letters, 2015. 37(7): p. 1447-1454. [2] Maruyama S , Nakagomi K , Tomizuka N , et al. Angiotensin I-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and the ileum of rats.[J]. Agricultural and Biological Chemistry, 1985, 49(5):1405-1409. [3] Matoba T , Nagayasu C , Hayashi R , et al. Bitter Peptides in Tryptic Hydrolysate of Casein[J]. Agricultural and Biological Chemistry, 1969, 33(11):1662-1663.
PubDate	2014